In vitro studies identified ClpC1 as the target of antituberculosis
compound cyclomarin
A (CymA), which could guide the design of
new ClpC1 inhibitors to treat tuberculosis. CymA has activity against both
replicating and nonreplicating tuberculosis, but the 848-amino-acid protein
has poor pharmacokinetics. Cocrystallization of CymA in complex with ClpC1
showed that the compound bound the N-terminal domain of ClpC1. Next steps
include designing ClpC1 inhibitors with improved therapeutic properties.

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